Research workbench
Catalytic domain from dihydrolipoamide succinyltransferase
Analyse Catalytic domain from dihydrolipoamide succinyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E2O
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoamide succinyltransferase
- EC
- 2.3.1.61
- UniProt
- P07016
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrolipoamide succinyltransferase (EC 2.3.1.61) | protein | 230 | 37% helix, 24% strand | P07016 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.43 | 0.73 | 28 | empty |
| 2 | 138 | 0.41 | 0.74 | 26 | empty |
Compared structures
- 1E2O · Catalytic domain from dihydrolipoamide succinyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P07016
- Elsewhere: RCSB PDB 1E2O · PDBe 1E2O · UniProt P07016
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